Antioxidant salmon collagen peptide and preparation method thereof

Abstract

The present invention discloses an antioxidant salmon collagen peptide and a preparation method thereof, belonging to the technical field of salmon collagen peptide processing. The present invention first enzymatically hydrolyzes salmon material with phospholipase A2 to hydrolyze the abundant membrane phospholipids in the salmon material, destroying the fat cell structure and releasing the encapsulated triglycerides. Aspergillus oryzae lipase is then used for a second enzymatic hydrolysis to hydrolyze the macromolecular lipids into free fatty acids that are easily soluble in supercritical carbon dioxide. Supercritical carbon dioxide extraction is then used to obtain defatted salmon material, greatly improving the lipid removal rate. Subsequently, collagen is extracted and enzymatically hydrolyzed to obtain antioxidant salmon collagen peptides with a smaller molecular weight and stronger antioxidant properties.

Description

Technical Field

[0001] The present invention relates to the technical field of salmon collagen peptide processing, and in particular to a method for preparing antioxidant salmon collagen peptide. Background Art

[0002] With the growing demand for functional foods and health ingredients, marine bioactive peptides are attracting attention due to their high nutritional value and physiological functions. Salmon is rich in collagen, and its enzymatic hydrolysis product, salmon collagen peptides (SCP), are easily absorbed and hypoallergenic. However, their natural antioxidant capacity is limited, making it difficult to meet the demand for efficient free radical scavenging.

[0003] Traditional methods to enhance antioxidant activity include: enzymatic optimization: selective hydrolysis through alkaline protease, trypsin, etc. to release antioxidant peptides containing specific amino acids (such as histidine and tyrosine); physical modification: such as ultrasonic treatment or high-pressure homogenization to expose active groups; chemical cross-linking: combining with polyphenols (such as tea polyphenols), but often faces problems of low binding rate or poor stability.

[0004] However, these methods have defects such as easily destroying protein structure and causing loss of product activity. Summary of the Invention

[0005] The main purpose of the present invention is to provide an antioxidant salmon collagen peptide and a preparation method thereof, so as to solve the technical problems in the prior art that the preparation of salmon collagen peptide is easy to destroy its structure and has poor antioxidant properties.

[0006] To achieve the above object, the present invention provides a method for preparing antioxidant salmon collagen peptide, comprising the following steps:

[0007] S10: The salmon feed is crushed into a slurry, phospholipase A2 is added for the first enzymatic hydrolysis, and then Aspergillus oryzae lipase is added for the second enzymatic hydrolysis. After the enzyme is inactivated, the feed is dried to a moisture content of less than 10%, and then placed in a supercritical extraction kettle, and subjected to supercritical CO2 extraction to obtain defatted salmon feed;

[0008] S20: mixing and stirring the defatted salmon material, the acetic acid solution, and the pepsin, then adding a NaCl solution for salting out, followed by centrifugation to obtain a precipitate, dissolving the precipitate with acetic acid, dialyzing, and spray drying for the first time to obtain salmon collagen;

[0009] S30: dissolving the salmon collagen to obtain a salmon collagen solution, adding alkaline protease to the salmon collagen solution for a third enzymatic hydrolysis, inactivating the enzyme, dialyzing, and spray drying for a second time to obtain salmon collagen peptides.

[0010] In some embodiments of the present invention, the added amount of phospholipase A2 is 1% to 2% of the mass of the salmon feed.

[0011] In some embodiments of the present invention, the added amount of the Aspergillus oryzae lipase is 1% to 2% of the mass of the salmon feed.

[0012] In some embodiments of the present invention, the temperature of the first enzymatic hydrolysis is 35°C to 45°C; the temperature of the second enzymatic hydrolysis is 40°C to 50°C.

[0013] In some embodiments of the present invention, the extraction process includes a first stage and a second stage, wherein the pressure of the first stage is 15MPa~20MPa and the temperature is 35℃~40℃; the pressure of the second stage is 30MPa~35MPa and the temperature is 50℃~55℃.

[0014] In some embodiments of the present invention, the flow rate of the supercritical CO2 is 40-60 g / min.

[0015] In some embodiments of the present invention, the supercritical CO2 contains citric acid.

[0016] In some embodiments of the present invention, the added amount of pepsin is 1% to 2% of the mass of the defatted salmon material.

[0017] In some embodiments of the present invention, after dissolving the salmon collagen to obtain the salmon collagen solution, the salmon collagen solution is irradiated using UV irradiation.

[0018] The present invention also provides a salmon collagen peptide, which is prepared by the above-mentioned method for preparing the antioxidant salmon collagen peptide.

[0019] The beneficial effects that can be achieved by the present invention are:

[0020] In the step of processing salmon material, the present invention first performs step-by-step enzymatic hydrolysis by phospholipase A2 and Aspergillus oryzae lipase to selectively hydrolyze triglycerides and phospholipids, and then combines it with supercritical CO2 extraction to achieve deep degreasing while retaining the integrity of salmon collagen, thereby ensuring the antioxidant property of subsequent salmon collagen peptides. Then, pepsin is selected for enzymatic hydrolysis under acidic conditions, and salting out and dialysis techniques are used to extract high-purity salmon collagen, avoiding the problem that traditional acid-base method of extracting collagen easily destroys the protein structure and the antioxidant property of subsequent collagen peptides. Then, alkaline protease is used to hydrolyze the salmon collagen to obtain antioxidant salmon collagen peptides with good antioxidant property and small molecular weight. BRIEF DESCRIPTION OF THE DRAWINGS

[0021] In order to more clearly illustrate the embodiments of the present invention or the technical solutions in the prior art, the following briefly introduces the drawings required for use in the embodiments or the description of the prior art. Obviously, the drawings described below are only some embodiments of the present invention. For ordinary technicians in this field, other drawings can be obtained based on the structures shown in these drawings without paying any creative work.

[0022] Figure 1 The present invention is a schematic diagram of the preparation process of an antioxidant salmon collagen peptide.

[0023] The purpose, features and advantages of the present invention will be further described with reference to the accompanying drawings and in conjunction with the embodiments. DETAILED DESCRIPTION

[0024] It should be understood that the specific embodiments described herein are only used to explain the present invention and are not intended to limit the present invention.

[0025] The following will clearly and completely describe the technical solutions in the embodiments of the present invention in conjunction with the accompanying drawings. Obviously, the described embodiments are only part of the embodiments of the present invention, not all of the embodiments. All other embodiments obtained by ordinary technicians in this field based on the embodiments of the present invention without making any creative efforts shall fall within the scope of protection of the present invention.

[0026] In the present invention, descriptions such as "first" and "second" are only used for descriptive purposes and cannot be understood as indicating or implying their relative importance or implicitly indicating the number of the indicated technical features. Therefore, the features defined as "first" and "second" may explicitly or implicitly include at least one of such features. In addition, the technical solutions between the various embodiments can be combined with each other, but they must be based on the ability of ordinary technicians in this field to implement them. When the combination of technical solutions is contradictory or cannot be implemented, it should be deemed that such a combination of technical solutions does not exist and is not within the scope of protection required by the present invention.

[0027] The present invention provides a preparation method of antioxidant salmon collagen peptide and salmon collagen peptide, referring to Figure 1 , the preparation method comprises the following steps:

[0028] S10: The salmon feed is crushed into a slurry, phospholipase A2 is added for the first enzymatic hydrolysis, and then Aspergillus oryzae lipase is added for the second enzymatic hydrolysis. After the enzyme is inactivated, the feed is dried to a moisture content of less than 10%, and then placed in a supercritical extraction kettle, and subjected to supercritical CO2 extraction to obtain defatted salmon feed;

[0029] S20: mixing and stirring the defatted salmon material, the acetic acid solution, and the pepsin, then adding a NaCl solution for salting out, followed by centrifugation to obtain a precipitate, dissolving the precipitate with acetic acid, dialyzing, and spray drying for the first time to obtain salmon collagen;

[0030] S30: dissolving the salmon collagen to obtain a salmon collagen solution, adding alkaline protease to the salmon collagen solution for a third enzymatic hydrolysis, inactivating the enzyme, dialyzing, and spray drying for a second time to obtain salmon collagen peptides.

[0031] In the step of processing salmon material, the present invention first performs step-by-step enzymatic hydrolysis using phospholipase A2 and Aspergillus oryzae lipase to selectively hydrolyze triglycerides and phospholipids, and then combines it with supercritical CO2 extraction to achieve deep degreasing while retaining the integrity of salmon collagen, thereby ensuring the antioxidant property of salmon collagen peptides. Subsequently, pepsin is selected for enzymatic hydrolysis under acidic conditions, and salting out and dialysis techniques are used to extract high-purity salmon collagen, avoiding the problem that traditional acid-base method of protein extraction easily destroys protein structure and antioxidant properties. Then, alkaline protease is used to hydrolyze salmon protein to obtain antioxidant salmon collagen peptides with good antioxidant properties and a small molecular weight.

[0032] Lipid substances in salmon feed usually have long-chain structures and ester bonds, which will reduce their compatibility with supercritical carbon dioxide. Therefore, before supercritical extraction, phospholipase A2 is used for the first enzymatic hydrolysis. Phospholipase A2 can hydrolyze the rich membrane phospholipids in salmon feed, destroy the fat cell structure, release the encapsulated triglycerides, and improve the enzymatic hydrolysis efficiency of triglycerides in the second enzymatic hydrolysis. Triglycerides are hydrolyzed into free fatty acids. Free fatty acids have a small molecular weight and low polarity. The carboxyl groups in them can form hydrogen bonds with the weak polarity of CO2, enhancing the solubility of lipid substances in CO2 and making them easier to be extracted by supercritical carbon dioxide, thereby achieving the effect of improving the removal of lipids while retaining the structural integrity of the protein, ensuring the antioxidant activity of the salmon collagen peptides prepared subsequently.

[0033] In step S10, the salmon material is broken into a slurry, which not only improves the enzymatic hydrolysis effect of lipase, but also increases the contact area with supercritical CO2 in the subsequent supercritical CO2 extraction process, thereby improving the removal rate of impurities such as lipid substances and fishy substances, obtaining salmon protein with higher purity, retaining its structural integrity, and retaining the antioxidant activity of the final product, salmon collagen peptide.

[0034] In some embodiments, the temperature of the first enzymolysis is 35°C to 45°C, the time of the first enzymolysis is 2h to 3h, the pH of the first enzymolysis is 6 to 8, the temperature of the second enzymolysis is 40°C to 50°C, the time of the second enzymolysis is 1h to 2h, and the pH of the second enzymolysis is 7 to 8. The present invention shortens the enzymolysis time by two enzymolysis treatments, which can solve the generation of bitter peptide taste caused by the enzymolysis time process. In this embodiment, the pH can be adjusted by adding phosphate buffer.

[0035] In some embodiments, the added amount of Aspergillus oryzae lipase is 1%~2% of the mass of the salmon feed, which can be 1%, 1.5%, 2%, etc., and the added amount of phospholipase A2 is 1%~2% of the mass of the salmon feed, which can be 1%, 1.5%, 2%, etc.

[0036] In some embodiments, the enzyme inactivation method of step S10 includes a pulse method, and the pulse intensity range is 1J / cm 2 ~5J / cm 2 It is beneficial to retain the heat-sensitive antioxidant components in salmon collagen peptides and is beneficial to some hydrophobic peptide segments, thereby ensuring the antioxidant properties of the product.

[0037] In some embodiments, the salmon material includes at least one of salmon meat, salmon bones, and salmon skin.

[0038] In some embodiments, after the salmon material is pulped, it can also be rinsed with a NaCl solution with a mass concentration of 1% to reduce the inhibition of hemoglobin on enzyme activity.

[0039] In some embodiments, the extraction process includes a first stage and a second stage. In the first stage, the pressure is 15MPa~20MPa and the temperature is 35℃~40℃, which is conducive to removing free lipids. In the second stage, the pressure is 30MPa~35MPa and the temperature is 50℃~55℃, which can effectively extract bound lipids. By combining the first stage of low temperature and low pressure with the second stage of high temperature and high pressure, the removal effect of lipid substances in salmon feed can be improved, while retaining the structural integrity of salmon collagen, thereby ensuring the antioxidant properties of the final product, salmon collagen peptide.

[0040] In some embodiments, the extraction time of the first stage is 1 hour to 2 hours, and the extraction time of the second stage is 1 hour to 2 hours.

[0041] In some embodiments, the flow rate of supercritical CO2 is 40 g / min to 60 g / min.

[0042] In some embodiments, adding a trace amount of citric acid to supercritical CO2 and controlling the pH of CO2 to 3-4 can inhibit the cross-linking of lipid oxidation products and proteins, reduce protein carbonylation, thereby improving the extraction effect of protein peptides and increasing the antioxidant properties of the product salmon collagen peptide.

[0043] In some embodiments, before performing step S20, the defatted salmon material is plasma treated, and the conditions for the plasma treatment are as follows: the power of the plasma treatment is 50w~100w, and the time of the plasma treatment is 2min~5min, which can loosen the collagen fiber structure of the defatted salmon material, improve the permeability of the pepsin in step S20, reduce the amount of enzyme used, or increase the extraction rate of salmon collagen under the condition of the same enzyme usage, thereby enhancing the extraction of salmon collagen peptides and enhancing the antioxidant properties of the final product.

[0044] In the present invention, the function of step S20 is to extract collagen from the salmon material.

[0045] In some embodiments, in the step of mixing the defatted salmon feed, acetic acid solution, and pepsin, the material-liquid ratio of the defatted salmon feed and the acetic acid solution is 100 g / 1 L, and the amount of pepsin added is 1% to 2% of the mass of the defatted salmon feed.

[0046] In some embodiments, the stirring temperature is 4° C., and the stirring time is 40 h to 50 h.

[0047] In some embodiments, the concentration of the NaCl solution for salting out is 2.5M to 3M.

[0048] In some embodiments, the centrifugal speed is 10,000-15,000 rpm, and the centrifugation time is 20 min-30 min.

[0049] In some embodiments, the concentration of acetic acid used to dissolve the precipitate is 0.1M to 0.2M.

[0050] In some embodiments, during the dialysis process, the molecular retention capacity is 3kDa~3.5kDa, and the dialysis time is 60h~72h, thereby achieving the purpose of removing impurities.

[0051] In the present invention, step S30 mainly involves enzymatically hydrolyzing the extracted collagen to obtain collagen peptides.

[0052] In some embodiments, salmon collagen can be dissolved in an acetic acid solution with a concentration of 0.1M~0.2M to obtain a salmon collagen solution, and the mass concentration of the salmon collagen solution can be 10g~20g / 100ml.

[0053] In some embodiments, the amount of alkaline protease added is 4% to 5% of the salmon collagen quality.

[0054] In some embodiments, the enzymatic hydrolysis temperature of the third enzymatic hydrolysis is 50° C. to 55° C., and the enzymatic hydrolysis time is 2 h to 3 h.

[0055] In some embodiments, during the dialysis process, the molecular retention capacity is 3kDa~3.5kDa, and the dialysis time is 40h~72h, thereby achieving the purpose of removing impurities.

[0056] In some embodiments, the enzyme inactivation method of step S30 includes a pulse method, wherein the pulse intensity range is 1J / cm 2 ~5J / cm 2 It is beneficial to retain the heat-sensitive antioxidant components in salmon collagen peptides and is beneficial to some hydrophobic peptide segments, thereby ensuring the antioxidant properties of the product.

[0057] In some embodiments, after dissolving the salmon collagen to obtain a salmon collagen solution, the salmon collagen solution is irradiated with UV radiation. Pre-treating the salmon collagen solution with UV radiation is beneficial for inducing protein oxidative folding, exposing hidden antioxidant groups, and enhancing the release of antioxidant active peptides during subsequent enzymatic hydrolysis, thereby improving the antioxidant properties of the final salmon collagen peptide product.

[0058] In some embodiments, the wavelength of UV irradiation is 254 nm, which is beneficial for exposing hidden protein disulfide bonds and aromatic amino acids and enhancing the release of antioxidant active peptides.

[0059] In some embodiments, the intensity of UV radiation is 10 mW / cm 2 ~15mW / cm 2 .

[0060] In some embodiments, the UV irradiation time is 5 min to 10 min.

[0061] In some embodiments, during UV irradiation, the frequency is 2 minutes of irradiation followed by a 1 minute pause, so that the temperature of the salmon collagen solution is ≤40°C to prevent overheating from damaging the structure of the protein.

[0062] In some embodiments, the irradiating lamp is 10 cm to 15 cm away from the salmon collagen solution to prevent excessive temperature from damaging the protein structure.

[0063] In some embodiments, after the UV irradiation treatment is completed, the salmon collagen solution is transferred to a light-proof container and stirred to dissipate heat.

[0064] The technical solutions of the present invention are further described in detail below in conjunction with specific embodiments. It should be understood that the following specific embodiments are only used to explain the present invention and are not used to limit the present invention.

[0065] Example 1

[0066] Example 1 The preparation method of antioxidant salmon collagen peptide is as follows:

[0067] S10: The salmon feed was crushed into a slurry, phospholipase A2 was added according to 1% of the mass of the salmon feed, the pH was adjusted to 6-8, and the first enzymatic hydrolysis was carried out at 40°C for 3 hours. Then, Aspergillus oryzae lipase was added according to 2% of the mass of the salmon feed, the pH was adjusted to 7-8, and the second enzymatic hydrolysis was carried out at 45°C for 1 hour. Then, the enzyme was heated at an intensity of 5J / cm 2 The enzyme was inactivated by pulsed strong light and dried to a moisture content of less than 10%. The mixture was then placed in a supercritical extraction kettle and subjected to supercritical CO2 extraction to obtain defatted salmon material. The conditions for supercritical extraction were as follows: the pressure in the first stage was controlled at 20 MPa and the temperature was 35°C. After extraction for 1 hour, the mixture was adjusted to the second stage. The pressure in the second stage was controlled at 30 MPa and the temperature was 55°C. The extraction time was 2 hours. The flow rate of CO2 was controlled at 60 g / min throughout the process. A trace amount of citric acid was added to the CO2 to control the pH of the input supercritical CO2 to 3~4.

[0068] S20: Dissolve the defatted salmon feed in a 0.1M acetic acid solution to obtain a defatted salmon feed solution with a concentration of 100g / 1L, and add pepsin according to 1% of the mass of the salmon feed. Stir at 4°C for 50h, then add a 3M NaCl solution for salting out, and then centrifuge at a speed of 15000 for 20min to obtain a precipitate. Dissolve the precipitate in 0.1M acetic acid and dialyze for 72h. The molecular weight intercepted by dialysis is 3.5kDa. Then spray dry to obtain salmon collagen.

[0069] S30: Dissolve salmon collagen in 1M acetic acid solution to obtain a salmon collagen solution with a mass concentration of 10g / 100ml, and add alkaline protease according to 4% of the mass of salmon collagen. Perform the third enzymatic hydrolysis at 50℃ for 2h, and then use an acetic acid solution with an intensity of 5J / cm 2 The enzyme was inactivated by pulsed strong light, followed by dialysis for 50 hours, the intercepted molecular weight was 3KDa, and then spray-dried to obtain salmon collagen peptide.

[0070] Example 2

[0071] Example 2 Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that the added amount of phospholipase A2 was 2%.

[0072] Example 3

[0073] Example 3 Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that the added amount of Aspergillus oryzae lipase was 1%.

[0074] Example 4

[0075] Example 4 Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that the amount of pepsin added was 2% of the mass of the defatted salmon material.

[0076] Example 5

[0077] Example 5 Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that citric acid was not added in step S10 to adjust the pH of supercritical CO2.

[0078] Example 6

[0079] Example 6 prepares antioxidant salmon collagen peptides with reference to the preparation method of Example 1, except that, in step S10, after obtaining defatted salmon material through supercritical CO2 extraction, Example 6 uses plasma equipment to perform plasma treatment on the defatted salmon material with a power of 100W and a time of 2 minutes.

[0080] Example 7

[0081] Example 7 Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that in step S30, the salmon collagen was dissolved in 1M acetic acid solution to obtain a salmon collagen solution, and then the salmon collagen solution was irradiated with UV irradiation. The irradiation lamp was 10 cm away from the salmon collagen solution, the irradiation wavelength was 254 nm, and the irradiation intensity was 10 mW / cm 2 The irradiation time is 8 minutes, and the irradiation frequency is 1 minute pause after every 2 minutes of irradiation to ensure that the temperature of the salmon gelatin solution is ≤40℃.

[0082] Comparative Example 1

[0083] Comparative Example 1 Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that phospholipase A2 was not added in step S10 for the first enzymatic hydrolysis.

[0084] Comparative Example 2

[0085] Comparative Example 2: Antioxidant salmon collagen peptide was prepared by referring to the preparation method of Example 1, except that Aspergillus oryzae lipase was not added in step S10 for the second enzymatic hydrolysis.

[0086] Performance Testing

[0087] Antioxidant performance test:

[0088] The salmon collagen peptides prepared in Examples 1 to 5 and Comparative Examples 1 to 2 were prepared into 10 mg / ml sample aqueous solutions. 200 μL of the sample solutions were added to a 96-well plate and mixed with an equal volume of 0.1 mmol / L DPPH ethanol solution. The mixture was reacted at room temperature in the dark for 30 minutes, and the absorbance of the reaction solution at 517 nm was measured.

[0089] Set up a control group: replace the DPPH ethanol solution in each group with anhydrous ethanol as the corresponding control group.

[0090] Set up blank groups: replace the sample aqueous solution in each group with deionized water as the corresponding blank group.

[0091] Set up the solvent group: a mixed solution of equal volumes of anhydrous ethanol and deionized water was used as the solvent group.

[0092] The absorbance of each reaction solution was measured respectively, and the calculation formula of DPPH free radical scavenging rate was as follows:

[0093] DPPH free radical scavenging rate (%) = 1-(A0-A2 / A1-A3) × 100%;

[0094] Among them, the experimental group was A0, the blank group was A1, the control group was A2, and the solvent group was A3.

[0095] Table 1

[0096]

[0097] It can be seen from Table 1 that the antioxidant salmon collagen peptide prepared by the method of the present invention has good antioxidant properties. Moreover, after the defatted salmon material is subjected to plasma treatment in Example 6, and after the salmon collagen solution is subjected to irradiation treatment in Example 7, the antioxidant properties of the salmon collagen peptide can be effectively improved.

[0098] The above are only preferred embodiments of the present invention and are not intended to limit the patent scope of the present invention. Any equivalent structure or equivalent process transformation made using the contents of the present invention description and drawings, or directly or indirectly applied in other related technical fields, are also included in the patent protection scope of the present invention.

Claims

1. A method for preparing antioxidant salmon collagen peptide, characterized in that: The following steps are involved: S10: The salmon feed is crushed into a slurry, phospholipase A2 is added for the first enzymatic hydrolysis, and then Aspergillus oryzae lipase is added for the second enzymatic hydrolysis. After the enzyme is inactivated, the feed is dried to a moisture content of less than 10%, and then placed in a supercritical extraction kettle, and subjected to supercritical CO2 extraction to obtain defatted salmon feed; S20: mixing and stirring the defatted salmon material, the acetic acid solution, and the pepsin, then adding a NaCl solution for salting out, followed by centrifugation to obtain a precipitate, dissolving the precipitate with acetic acid, dialyzing, and spray drying for the first time to obtain salmon collagen; S30: dissolving the salmon collagen to obtain a salmon collagen solution, adding alkaline protease to the salmon collagen solution for a third enzymatic hydrolysis, inactivating the enzyme, dialyzing, and spray drying for a second time to obtain salmon collagen peptides; The amount of phospholipase A2 added is 1% to 2% of the mass of the salmon feed; The amount of Aspergillus oryzae lipase added is 1% to 2% of the mass of the salmon feed; The temperature of the first enzymatic hydrolysis is 35°C to 45°C; the temperature of the second enzymatic hydrolysis is 40°C to 50°C; The extraction process includes a first stage and a second stage, wherein the pressure of the first stage is 15MPa-20MPa and the temperature is 35°C-40°C; the pressure of the second stage is 30MPa-35MPa and the temperature is 50°C-55°C; The flow rate of the supercritical CO2 is 40g / min~60g / min; The supercritical CO2 contains citric acid; The amount of pepsin added is 1% to 2% of the mass of the defatted salmon material; After dissolving the salmon collagen to obtain a salmon collagen solution, irradiating the salmon collagen solution with UV irradiation; The wavelength of the UV radiation is 254 nm, and the intensity of the UV radiation is 10 mW / cm 2 ~15mW / cm 2 The UV irradiation time is 5 minutes to 10 minutes, and the frequency is irradiation for 2 minutes and pause for 1 minute. During the UV irradiation process, the temperature of the salmon collagen solution is ≤40°C, and the irradiation lamp is 10 cm to 15 cm away from the salmon collagen solution.

2. A salmon collagen peptide, characterized in that: The salmon collagen peptide is prepared by the preparation method of the antioxidant salmon collagen peptide according to claim 1.

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